1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
This is an abbreviated version!
For detailed information about 3,4-dihydroxyphenylacetate 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.15
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1.13.11.15
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extradiol
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catecholate
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4-nitrocatechol
-
fuscum
-
brevibacterium
-
globiformis
-
manganese-dependent
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ring-cleaving
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extradiol-cleaving
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second-sphere
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monoanionic
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hydroperoxo
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4-hydroxyphenylacetate
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superoxo
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alkylperoxo
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feiii-superoxo
-
manganeseii
-
ortho-dihydroxylated
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side-on
-
crystallo
- 1.13.11.15
-
extradiol
-
catecholate
- 4-nitrocatechol
- fuscum
-
brevibacterium
- globiformis
-
manganese-dependent
-
ring-cleaving
-
extradiol-cleaving
-
second-sphere
-
monoanionic
-
hydroperoxo
- 4-hydroxyphenylacetate
-
superoxo
-
alkylperoxo
-
feiii-superoxo
-
manganeseii
-
ortho-dihydroxylated
-
side-on
-
crystallo
Reaction
Synonyms
2,3-HPCD, 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, Bf 2,3-HPCD, DHPAO, Fe-HPCD, Fe-MndD, FeHPCD, homoprotocatechuate 2,3 dioxygenase, homoprotocatechuate 2,3-dioxygenase, homoprotocatechuate dioxygenase, HPADO, HPC 2,3-dioxygenase, HPC dioxygenase, HPCA 2,3-dioxygenase, HPCD, Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn-HPCD, Mn-MndD, MndD, MnHPCD, oxygenase, homoprotocatechuate 2,3-di-, PaDHPAO
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Reference
Reference on EC 1.13.11.15 - 3,4-dihydroxyphenylacetate 2,3-dioxygenase
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Blakley, E.R.
The catabolism of L-tyrosine by an Arthrobacter sp.
Can. J. Microbiol.
23
1128-1139
1977
Arthrobacter sp.
Cooper, R.A.; Skinner, M.A.
Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli
J. Bacteriol.
143
302-306
1980
Escherichia coli
Barbour, M.G.; Bayly, R.C.
Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida
J. Bacteriol.
147
844-850
1981
Pseudomonas putida
Klages, U.; Markus, A.; Lingens, F.
Degradation of 4-chlorophenylacetic acid by a Pseudomonas species
J. Bacteriol.
146
64-68
1981
Pseudomonas sp., Pseudomonas sp. CBS3
Jenkins, J.R.; Cooper, R.A.
Molecular cloning, expression, and analysis of the genes of the homoprotocatechuate catabolic pathway of Escherichia coli C
J. Bacteriol.
170
5317-5324
1988
Escherichia coli, Escherichia coli C
Nozaki, M.
Nonheme iron dioxygenase
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
135-165
1974
Pseudomonas putida
-
Adachi, K.; Takeda, Y.; Senoh, S.; Kita, H.
Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis
Biochim. Biophys. Acta
93
483-493
1964
Pseudomonas putida
Barbour, M.G.; Bayly, R.C.
Regulation of the 4-hydroxyphenylacetic acid meta-cleavage pathway in an Acinetobacter sp
Biochem. Biophys. Res. Commun.
79
663-670
1977
Acinetobacter sp., Acinetobacter sp. 3B-1
Barbour, M.G.; Bayly, R.C.
Regulation of the meta-cleavage of 4-hydroxyphenylacetic acid by Pseudomonas putida
Biochem. Biophys. Res. Commun.
76
565-571
1977
Pseudomonas putida
Lee, Y.L.; Dagley, S.
Comparison of two dioxygenases from Pseudomonas putida
J. Bacteriol.
131
1016-1017
1977
Pseudomonas putida
Roper, D.I.; Cooper, R.A.
Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C
FEBS Lett.
275
53-57
1990
Escherichia coli
Kutty, R.K.; Devi, N.A.; Veeraswamy, M.; Ramesh, S.; Rao, P.V.S.
Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde
Biochem. J.
167
163-170
1977
Arthrobacter synephrinum
Mayer, R.; Widom, J.; Que, L.
Involvement of superoxide in the reactions of the catechol dioxygenases
Biochem. Biophys. Res. Commun.
92
285-291
1980
Brevibacillus brevis
Que, L.; Widom, J.; Crawford, R.L.
3,4-Dihydroxyphenylacetate 2,3-dioxygenase. A manganese(II) dioxygenase from Bacillus brevis
J. Biol. Chem.
256
10941-10944
1981
Brevibacillus brevis
Lee, C.W.; Lucas, S.; Desmazeaud, M.J.
Phenylalanine and tyrosine catabolism in some cheese coryneform bacteria
FEMS Microbiol. Lett.
26
201-205
1985
Brevibacterium linens
-
Trias, J.; Vinas, M.; Guinea, J.; Loren, J.G.
Isolation from urine of two Serratia marcescens strains excreting a diffusible yellow pigment
J. Gen. Microbiol.
133
773-777
1987
Serratia marcescens
Cuskey, S.M.; Olsen, R.H.
Catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO1 via meta cleavage of homoprotocatechuic acid
J. Bacteriol.
170
393-399
1988
Pseudomonas aeruginosa
Jamaluddin, M.P.
Purification and properties of homoprotocatechuate 2,3-dioxygenase from Bacillus stearothermophilus
J. Bacteriol.
129
690-697
1977
Geobacillus stearothermophilus
Sparnins, V.L.; Chapman, P.J.
Catabolism of L-tyrosine by the homoprotocatechuate pathway in gram-positive bacteria
J. Bacteriol.
127
362-366
1976
Corynebacterium sp., Micrococcus luteus, Micrococcus sp., Nocardia globerula, Rhodococcus rhodnii, Nocardia globerula CL-1
Sparnins, V.L.; Chapman, P.J.; Dagley, S.
Bacterial degradation of 4-hydroxyphenylacetic acid and homoprotocatechuic acid
J. Bacteriol.
120
159-167
1974
Acinetobacter sp., Pseudomonas sp.
Ono-Kamimoto, M.
Studies on 3,4-dihydroxyphenylacetate 2,3-dioxygenase. I. Role of iron, substrate binding, and some other properties
J. Biochem.
74
1049-1059
1973
Pseudomonas putida
Ono-Kamimoto, M.; Senoh, S.
Studies on 3,4-dihydroxyphenylacetate-2,3-dioxygenase. II. Role of sulfhydryl groups and subunit structure
J. Biochem.
75
321-331
1974
Pseudomonas putida
Miller, M.A.; Lipscomb, J.D.
Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity
J. Biol. Chem.
271
5524-5535
1996
Brevibacterium fuscum
Boldt, Y.R.; Whiting, A.K.; Wagner, M.L.; Sadowsky, M.J.; Que, L.Jr.; Wackett, L.P.
Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2
Biochemistry
36
2147-2153
1997
Arthrobacter globiformis, Arthrobacter globiformis CM-2
Wang, Y.Z.; Lipscomb, J.D.
Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum
Protein Expr. Purif.
10
1-9
1997
Brevibacterium fuscum
Gibello, A.; Ferrer, E.; Martin, M.; Garrido-Pertierra, A.
3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Klebsiella pneumoniae, a Mg2+-containing dioxygenase involved in aromatic catabolism
Biochem. J.
301
145-150
1994
Klebsiella pneumoniae
-
Groce, S.L.; Miller-Rodeberg, M.A.; Lipscomb, J.D.
Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
Biochemistry
43
15141-15153
2004
Brevibacterium fuscum
Groce, S.L.; Lipscomb, J.D.
Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme
J. Am. Chem. Soc.
125
11780-11781
2003
Brevibacterium fuscum
Vetting, M.W.; Wackett, L.P.; Que, L.Jr.; Lipscomb, J.D.; Ohlendorf, D.H.
Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases
J. Bacteriol.
186
1945-1958
2004
Arthrobacter globiformis, Brevibacterium fuscum
Groce, S.L.; Lipscomb, J.D.
Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates
Biochemistry
44
7175-7188
2005
Brevibacterium fuscum
Emerson, J.P.; Wagner, M.L.; Reynolds, M.F.; Que, L.; Sadowsky, M.J.; Wackett, L.P.
The role of histidine 200 in MndD, the Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis CM-2, a site-directed mutagenesis study
J. Biol. Inorg. Chem.
10
751-760
2005
Arthrobacter globiformis, Arthrobacter globiformis CM-2
Xu, L.; Zhao, W.; Wang, X.
Finding molecular dioxygen tunnels in homoprotocatechuate 2,3-dioxygenase: implications for different reactivity of identical subunits
Eur. Biophys. J.
39
327-336
2009
Brevibacterium fuscum (Q45135)
Georgiev, V.; Borowski, T.; Blomberg, M.R.; Siegbahn, P.E.
A comparison of the reaction mechanisms of iron- and manganese-containing 2,3-HPCD: an important spin transition for manganese
J. Biol. Inorg. Chem.
13
929-940
2008
Brevibacterium fuscum (Q45135), Brevibacterium fuscum
Xu, L.; Liu, X.; Zhao, W.; Wang, X.
Locally enhanced sampling study of dioxygen diffusion pathways in homoprotocatechuate 2,3-dioxygenase
J. Phys. Chem. B
113
13596-13603
2009
Brevibacterium fuscum (Q45135)
Emerson, J.P.; Kovaleva, E.G.; Farquhar, E.R.; Lipscomb, J.D.; Que, L.
Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state
Proc. Natl. Acad. Sci. USA
105
7347-7352
2008
Arthrobacter globiformis, Brevibacterium fuscum
Mbughuni, M.M.; Chakrabarti, M.; Hayden, J.A.; Bominaar, E.L.; Hendrich, M.P.; Muenck, E.; Lipscomb, J.D.
Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme
Proc. Natl. Acad. Sci. USA
107
16788-16793
2010
Brevibacterium fuscum
Mbughuni, M.M.; Chakrabarti, M.; Hayden, J.A.; Meier, K.K.; Dalluge, J.J.; Hendrich, M.P.; Muenck, E.; Lipscomb, J.D.
Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates
Biochemistry
50
10262-10274
2011
Brevibacterium fuscum
Mbughuni, M.M.; Meier, K.K.; Muenck, E.; Lipscomb, J.D
Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant
Biochemistry
51
8743-8754
2012
Brevibacterium fuscum
Kovaleva, E.G.; Lipscomb, J.D.
Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation
Biochemistry
51
8755-8763
2012
Brevibacterium fuscum (Q45135)
Henderson, K.L.; Le, V.H.; Lewis, E.A.; Emerson, J.P.
Exploring substrate binding in homoprotocatechuate 2,3-dioxygenase using isothermal titration calorimetry
J. Biol. Inorg. Chem.
17
991-994
2012
Brevibacterium fuscum
Hayden, J.A.; Farquhar, E.R.; Que, L.; Lipscomb, J.D.; Hendrich, M.P.
NO binding to Mn-substituted homoprotocatechuate 2,3-dioxygenase: relationship to O2 reactivity
J. Biol. Inorg. Chem.
18
717-728
2013
Brevibacterium fuscum
Mendez, V.; Agullo, L.; Gonzalez, M.; Seeger, M.
The homogentisate and homoprotocatechuate central pathways are involved in 3- and 4-hydroxyphenylacetate degradation by Burkholderia xenovorans LB400
PLoS ONE
6
e17583
2011
Paraburkholderia xenovorans
Pornsuwan, S.; Maenpuen, S.; Kamutira, P.; Watthaisong, P.; Thotsaporn, K.; Tongsook, C.; Juttulapa, M.; Nijvipakul, S.; Chaiyen, P.
3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Pseudomonas aeruginosa an Fe(II)-containing enzyme with fast turnover
PLoS ONE
12
e0171135
2017
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO
Bauri, S.; Sen, M.; Das, R.; Mondal, S.
In-silico investigation of the efficiency of microbial dioxygenases in degradation of sulfonylurea group herbicides
Bioremediat. J.
26
76-87
2022
Arthrobacter globiformis (Q44048), Brevibacterium fuscum (Q45135)
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